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Title: Fine Tuning of Redox Networks on Multiheme Cytochromes from Geobacter sulfurreducens Drives Physiological Electron/Proton Energy Transduction

Abstract

The bacteriumGeobacter sulfurreducens (Gs)can grow in the presence of extracellular terminal acceptors, a property that is currently explored to harvest electricity from aquatic sediments and waste organic matter into microbial fuel cells. A family composed of five triheme cytochromes (PpcA-E) was identified inGs. These cytochromes play a crucial role by bridging the electron transfer from oxidation of cytoplasmic donors to the cell exterior and assisting the reduction of extracellular terminal acceptors. The detailed thermodynamic characterization of such proteins showed that PpcA and PpcD have an important redox-Bohr effect that might implicate these proteins in the e-/H+coupling mechanisms to sustain cellular growth. The physiological relevance of the redox-Bohr effect in these proteins was studied by determining the fractional contribution of each individual redox-microstate at different pH values. For both proteins, oxidation progresses from a particular protonated microstate to a particular deprotonated one, over specific pH ranges. The preferred e-/H+transfer pathway established by the selected microstates indicates that both proteins are functionally designed to couple e-/H+transfer at the physiological pH range for cellular growth.

Authors:
 [1];  [1];  [2];  [3];  [1]
  1. Universidade Nova de Lisboa, Campus Caparica, Caparica (Portugal). Faculdade de Ciências e Tecnologia. Departamento de Química. Requimte-CQFB
  2. Instituto de Química-Física “Rocasolano”, Madrid (Spain). CSIC. Departamento de Espectroscopía y Estructura Molecular
  3. Argonne National Lab. (ANL), Argonne, IL (United States)
Publication Date:
Research Org.:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
OSTI Identifier:
1626203
Grant/Contract Number:  
AC02-06CH11357
Resource Type:
Accepted Manuscript
Journal Name:
Bioinorganic Chemistry and Applications
Additional Journal Information:
Journal Volume: 2012; Journal ID: ISSN 1565-3633
Publisher:
Hindawi
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Biochemistry & Molecular Biology; Chemistry

Citation Formats

Morgado, Leonor, Dantas, Joana M., Bruix, Marta, Londer, Yuri Y., and Salgueiro, Carlos A. Fine Tuning of Redox Networks on Multiheme Cytochromes from Geobacter sulfurreducens Drives Physiological Electron/Proton Energy Transduction. United States: N. p., 2012. Web. doi:10.1155/2012/298739.
Morgado, Leonor, Dantas, Joana M., Bruix, Marta, Londer, Yuri Y., & Salgueiro, Carlos A. Fine Tuning of Redox Networks on Multiheme Cytochromes from Geobacter sulfurreducens Drives Physiological Electron/Proton Energy Transduction. United States. https://doi.org/10.1155/2012/298739
Morgado, Leonor, Dantas, Joana M., Bruix, Marta, Londer, Yuri Y., and Salgueiro, Carlos A. Sun . "Fine Tuning of Redox Networks on Multiheme Cytochromes from Geobacter sulfurreducens Drives Physiological Electron/Proton Energy Transduction". United States. https://doi.org/10.1155/2012/298739. https://www.osti.gov/servlets/purl/1626203.
@article{osti_1626203,
title = {Fine Tuning of Redox Networks on Multiheme Cytochromes from Geobacter sulfurreducens Drives Physiological Electron/Proton Energy Transduction},
author = {Morgado, Leonor and Dantas, Joana M. and Bruix, Marta and Londer, Yuri Y. and Salgueiro, Carlos A.},
abstractNote = {The bacteriumGeobacter sulfurreducens (Gs)can grow in the presence of extracellular terminal acceptors, a property that is currently explored to harvest electricity from aquatic sediments and waste organic matter into microbial fuel cells. A family composed of five triheme cytochromes (PpcA-E) was identified inGs. These cytochromes play a crucial role by bridging the electron transfer from oxidation of cytoplasmic donors to the cell exterior and assisting the reduction of extracellular terminal acceptors. The detailed thermodynamic characterization of such proteins showed that PpcA and PpcD have an important redox-Bohr effect that might implicate these proteins in the e-/H+coupling mechanisms to sustain cellular growth. The physiological relevance of the redox-Bohr effect in these proteins was studied by determining the fractional contribution of each individual redox-microstate at different pH values. For both proteins, oxidation progresses from a particular protonated microstate to a particular deprotonated one, over specific pH ranges. The preferred e-/H+transfer pathway established by the selected microstates indicates that both proteins are functionally designed to couple e-/H+transfer at the physiological pH range for cellular growth.},
doi = {10.1155/2012/298739},
journal = {Bioinorganic Chemistry and Applications},
number = ,
volume = 2012,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2012},
month = {Sun Jan 01 00:00:00 EST 2012}
}

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